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Human Metabolome Database Version 2.5

 

Showing metabocard for Leukotriene C4 (HMDB01198)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:37
Accession Number HMDB01198
Secondary Accession Numbers HMDB06015
Common Name Leukotriene C4
Description Leukotriene C4 (LTC4) is a cysteinyl leukotriene (CysLT), a family of potent inflammatory mediators. Eosinophils, one of the principal cell types recruited to and activated at sites of allergic inflammation, is capable of elaborating lipid mediators, including leukotrienes derived from the oxidative metabolism of arachidonic acid (AA). Potentially 'activated' eosinophils may elaborate greater quantities of LTC4, than normal eosinophils. These activated eosinophils thus are 'primed' for enhanced LTC4 generation in response to subsequent stimuli. Some recognized priming stimuli are chemoattractants (e.g., eotaxin, PAF) that may participate in the recruitment of eosinophils to sites of allergic inflammation. The mechanisms by which chemoattractants and other activating cytokines (e.g., interleukin (IL)-5) or extracellular matrix components (e.g., fibronectin) enhance eosinophil eicosanoid formation are pertinent to the functions of these eicosanoids as paracrine mediators of allergic inflammation. Some eosinophil-derived eicosanoids may be active in down-regulating inflammation. It is increasingly likely that eicosanoids synthesized within cells, including eosinophils, may have intracellular (e.g., intracrine) roles in regulating cell functions, in addition to the more recognized activities of eicosanoids as paracrine mediators of inflammation. Acting extracellularly, the cysteinyl leukotrienes (CysLTs) LTC4 and its extracellular derivatives, LTD4 and LTE4 are key paracrine mediators pertinent to asthma and allergic diseases. Based on their receptor-mediated capabilities, they can elicit bronchoconstriction, mucous hypersecretion, bronchial hyperresponsiveness, increased microvascular permeability, and additional eosinophil infiltration. Eosinophils are a major source of CysLTs and have been identified as the principal LTC4 synthase expressing cells in bronchial mucosal biopsies of asthmatic subjects. (PMID: 12895596) Leukotrienes are eicosanoids. The eicosanoids consist of the prostaglandins (PGs), thromboxanes (TXs), leukotrienes (LTs) and lipoxins (LXs). The PGs and TXs are collectively identified as prostanoids. Prostaglandins were originally shown to be synthesized in the prostate gland, thromboxanes from platelets (thrombocytes) and leukotrienes from leukocytes, hence the derivation of their names. All mammalian cells except erythrocytes synthesize eicosanoids. These molecules are extremely potent, able to cause profound physiological effects at very dilute concentrations. All eicosanoids function locally at the site of synthesis, through receptor-mediated G-protein linked signaling pathways.
Synonyms
  1. (R-(R*,S*-(E,E,Z,Z)))-N-(S-(1-(4-carboxy-1-hydroxybutyl)-2,4,6,9-pentadecatetraenyl)-N-L-gamma-glutamyl-L-cysteinyl)-Glycine
  2. 5S,6R-Ltc
  3. 5S-hydroxy,6R-(S-glutathionyl),7E,9E,11Z,14Z-eicosatetraenoate
  4. 5S-hydroxy,6R-(S-glutathionyl),7E,9E,11Z,14Z-eicosatetraenoic acid
  5. L-gamma-glutamyl-S-[(1R,2E,4E,6Z,9Z)-1-[(1S)-4-carboxy-1-hydroxybutyl]-2,4,6,9-pentadecatetraenyl]-L-cysteinyl-glycine
  6. LTC
  7. LTC4
  8. Leucotriene C4
  9. Leukotriene C
  10. Leukotriene C1
  11. Leukotriene C4
  12. [R-[R*,S*-(E,E,Z,Z)]]-N-[S-[1-(4-carboxy-1-hydroxybutyl)-2,4,6,9-pentadecatetraenyl]-N-L-gamma-glutamyl-L-cysteinyl]-Glycine 5S,6R-LTC4
Chemical IUPAC Name 6-[2-(4-amino-4-carboxy-butanoyl)amino-2-(carboxymethylcarbamoyl)ethyl]sulfanyl-5-hydroxy-icosa-7,9,11,14-tetraenoic acid
Chemical Formula C30H47N3O9S
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Fatty acids
Class
  • Eicosanoids
Sub Class
  • Leukotrienes
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • thioether
  • primary amine
  • primary aliphatic amine (alkylamine)
  • carboxylic acid
  • secondary carboxylic acid amide
  • alkene
  • alpha-aminoacid
Biofunction
  • Component of Prostaglandin and leukotriene metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 625.774
Monoisotopic Molecular Weight 625.303284
Isomeric SMILES CCCCCC=C/CC=C/C=C/C=C/[C@@H](SC[C@H](NC(=O)CC[C@H](N)C(O)=O)C(=O)NCC(O)=O)[C@@H](O)CCCC(O)=O
Canonical SMILES CCCCCC=CCC=CC=CC=CC(SCC(NC(=O)CCC(N)C(O)=O)C(=O)NCC(O)=O)C(O)CCCC(O)=O
KEGG Compound ID C02166 Link Image
BioCyc ID LEUKOTRIENE-C4 Link Image
BiGG ID 2212273 Link Image
Wikipedia Link Leukotriene C4 Link Image
NuGOwiki Link HMDB01198 Link Image
Metagene Link HMDB01198 Link Image
METLIN ID 3681 Link Image
PubChem Compound 5280493 Link Image
PubChem Substance 7978470 Link Image
ChEBI ID 16978 Link Image
CAS Registry Number 72025-60-6
InChI Identifier InChI=1/C30H47N3O9S/c1-2-3-4-5-6-7-8-9-10-11-12-13-16-25(24(34)15-14-17-27(36)37)43-21-23(29(40)32-20-28(38)39)33-26(35)19-18-22(31)30(41)42/h6-7,9-13,16,22-25,34H,2-5,8,14-15,17-21,31H2,1H3,(H,32,40)(H,33,35)(H,36,37)(H,38,39)(H,41,42)/b7-6-,10-9-,12-11+,16-13+/t22-,23-,24-,25+/m0/s1
Synthesis Reference Rokach, Joshua; Young, Robert N.; Kakushima, Masatoshi; Lau, Cheuk-Kun; Seguin, Rick; Frenette, Richard; Guindon, Yvan. Synthesis of leukotrienes. New synthesis of natural leukotriene A4. Tetrahedron Letters (1981), 22(11), 979-82.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 2.54e-03 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -2
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 0.04 [Predicted by ALOGPS]; -2.031 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from LogP)
  • endoplasmic reticulum
  • Extracellular
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
Tissue Location
Tissue References
Intestine —
Lens —
Leukocyte —
Neutrophil —
Platelet —
Skin —
Smooth Muscle —
Concentrations (Normal)
Biofluid Blood
Value 0.00006 +/- 0.00003 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Hua Z, Fei H, Mingming X: Evaluation and interference of serum and skin lesion levels of leukotrienes in patients with eczema. Prostaglandins Leukot Essent Fatty Acids. 2006 Jul;75(1):51-5. Epub 2006 Jun 6. [PubMed Link Image]
Biofluid Blood
Value 0.001359 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Wishart DS, Knox C, Guo AC, Eisner R, Young N, Gautam B, Hau DD, Psychogios N, Dong E, Bouatra S, Mandal R, Sinelnikov I, Xia J, Jia L, Cruz JA, Lim E, Sobsey CA, Shrivastava S, Huang P, Liu P, Fang L, Peng J, Fradette R, Cheng D, Tzur D, Clements M, Lewis A, De Souza A, Zuniga A, Dawe M, Xiong Y, Clive D, Greiner R, Nazyrova A, Shaykhutdinov R, Li L, Vogel HJ, Forsythe I: HMDB: a knowledgebase for the human metabolome. Nucleic Acids Res. 2008 Oct 25. [PubMed Link Image]
  • Psychogios N, Hau DD, Peng J, Guo AC, Mandal R, Bouatra S, Sinelnikov I, Krishnamurthy R, Eisner R, Gautam B, Young N, Xia J, Knox C, Dong E, Huang P, Hollander Z, Pedersen TL, Smith SR, Bamforth F, Greiner R, McManus B, Newman JW, Goodfriend T, Wishart DS: The human serum metabolome. PLoS One. 2011 Feb 16;6(2):e16957. [PubMed Link Image]
Biofluid Blood
Value 4.7E-5 +/- 2.3E-5 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Quehenberger O, Armando AM, Brown AH, Milne SB, Myers DS, Merrill AH, Bandyopadhyay S, Jones KN, Kelly S, Shaner RL, Sullards CM, Wang E, Murphy RC, Barkley RM, Leiker TJ, Raetz CR, Guan Z, Laird GM, Six DA, Russell DW, McDonald JG, Subramaniam S, Fahy E, Dennis EA: Lipidomics reveals a remarkable diversity of lipids in human plasma. J Lipid Res. 2010 Nov;51(11):3299-305. Epub 2010 Jul 29. [PubMed Link Image]
Biofluid CSF
Value 6.989e-05 +/- 2.767e-05 uM
Age N/A
Sex N/A
Patient information Normal
Comments Not Available
References
  • Mayatepek E, Meissner T, Grobe H: Acute metabolic crisis with extreme deficiency of glutathione in combination with decreased levels of leukotriene C4 in a patient with glutathione synthetase deficiency. J Inherit Metab Dis. 2004;27(2):297-9. [PubMed Link Image]
Biofluid CSF
Value 0.000133 +/- 3.454e-05 uM
Age Children:1-13 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Matsuo M, Hamasaki Y, Masuyama T, Ohta M, Miyazaki S: Leukotriene B4 and C4 in cerebrospinal fluid from children with meningitis and febrile seizures. Pediatr Neurol. 1996 Feb;14(2):121-4. [PubMed Link Image]
Biofluid CSF
Value 0.000280 uM
Age N/A
Sex N/A
Patient information HIV-Seropositive (Neurologically normal)
Comments Not Available
References
  • Griffin DE, Wesselingh SL, McArthur JC: Elevated central nervous system prostaglandins in human immunodeficiency virus-associated dementia. Ann Neurol. 1994 May;35(5):592-7. [PubMed Link Image]
Biofluid CSF
Value 0.000101 uM
Age N/A
Sex N/A
Patient information Normal
Comments Not Available
References
  • Froldi M, Castagna A, Parma M, Piona A, Tedeschi A, Miadonna A, Lorini M, Orazio EN, Lazzarin A: Mediator release in cerebrospinal fluid of human immunodeficiency virus-positive patients with central nervous system involvement. J Neuroimmunol. 1992 May;38(1-2):155-61. [PubMed Link Image]
Biofluid CSF
Value 7.996e-05 uM
Age N/A
Sex N/A
Patient information Normal
Comments Not Available
References
  • Froldi M, Castagna A, Parma M, Piona A, Tedeschi A, Miadonna A, Lorini M, Orazio EN, Lazzarin A: Mediator release in cerebrospinal fluid of human immunodeficiency virus-positive patients with central nervous system involvement. J Neuroimmunol. 1992 May;38(1-2):155-61. [PubMed Link Image]
Biofluid CSF
Value 1.791e-05 +/- 4.798e-06 uM
Age N/A
Sex N/A
Patient information Normal
Comments Not Available
References
  • Nishisho T, Tonai T, Tamura Y, Ikata T: Experimental and clinical studies of eicosanoids in cerebrospinal fluid after spinal cord injury. Neurosurgery. 1996 Nov;39(5):950-6; discussion 956-7. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Blood
Value 0.00024 +/- 0.000065 uM
Age Adult:>18 yrs old
Sex Both
Condition Eczema
Comments Not Available
References
  • Hua Z, Fei H, Mingming X: Evaluation and interference of serum and skin lesion levels of leukotrienes in patients with eczema. Prostaglandins Leukot Essent Fatty Acids. 2006 Jul;75(1):51-5. Epub 2006 Jun 6. [PubMed Link Image]
Biofluid CSF
Value 0.000557 uM
Age N/A
Sex N/A
Comments Not Available
References
  • Froldi M, Castagna A, Parma M, Piona A, Tedeschi A, Miadonna A, Lorini M, Orazio EN, Lazzarin A: Mediator release in cerebrospinal fluid of human immunodeficiency virus-positive patients with central nervous system involvement. J Neuroimmunol. 1992 May;38(1-2):155-61. [PubMed Link Image]
Biofluid CSF
Value 0.000185 +/- 7.628e-05 uM
Age Children:1-13 yrs old
Sex N/A
Comments Not Available
References
  • Matsuo M, Hamasaki Y, Masuyama T, Ohta M, Miyazaki S: Leukotriene B4 and C4 in cerebrospinal fluid from children with meningitis and febrile seizures. Pediatr Neurol. 1996 Feb;14(2):121-4. [PubMed Link Image]
Biofluid CSF
Value <7.996e-05 uM
Age N/A
Sex N/A
Comments Not Available
References
  • Westcott JY, Murphy RC, Stenmark K: Eicosanoids in human ventricular cerebrospinal fluid following severe brain injury. Prostaglandins. 1987 Dec;34(6):877-87. [PubMed Link Image]
Biofluid CSF
Value 1.343e-05 uM
Age Adult:>18 yrs old
Sex Male
Comments Not Available
References
  • Mayatepek E, Meissner T, Grobe H: Acute metabolic crisis with extreme deficiency of glutathione in combination with decreased levels of leukotriene C4 in a patient with glutathione synthetase deficiency. J Inherit Metab Dis. 2004;27(2):297-9. [PubMed Link Image]
Biofluid CSF
Value <7.996e-05 uM
Age N/A
Sex N/A
Comments Not Available
References
  • Westcott JY, Murphy RC, Stenmark K: Eicosanoids in human ventricular cerebrospinal fluid following severe brain injury. Prostaglandins. 1987 Dec;34(6):877-87. [PubMed Link Image]
Biofluid CSF
Value 0.000422 uM
Age N/A
Sex N/A
Comments Not Available
References
  • Froldi M, Castagna A, Parma M, Piona A, Tedeschi A, Miadonna A, Lorini M, Orazio EN, Lazzarin A: Mediator release in cerebrospinal fluid of human immunodeficiency virus-positive patients with central nervous system involvement. J Neuroimmunol. 1992 May;38(1-2):155-61. [PubMed Link Image]
Biofluid CSF
Value 2.399e-05 uM
Age N/A
Sex N/A
Comments Not Available
References
  • Griffin DE, Wesselingh SL, McArthur JC: Elevated central nervous system prostaglandins in human immunodeficiency virus-associated dementia. Ann Neurol. 1994 May;35(5):592-7. [PubMed Link Image]
Biofluid CSF
Value <0.000160 uM
Age N/A
Sex N/A
Comments Not Available
References
  • Westcott JY, Murphy RC, Stenmark K: Eicosanoids in human ventricular cerebrospinal fluid following severe brain injury. Prostaglandins. 1987 Dec;34(6):877-87. [PubMed Link Image]
Biofluid CSF
Value 0.00413 +/- 0.000611 uM
Age N/A
Sex N/A
Comments Not Available
References
  • Rodriguez y Baena R, Gaetani P, Paoletti P: A study on cisternal CSF levels of arachidonic acid metabolites after aneurysmal subarachnoid hemorrhage. J Neurol Sci. 1988 Apr;84(2-3):329-35. [PubMed Link Image]
Biofluid CSF
Value 0.00130 +/- 0.000227 uM
Age N/A
Sex N/A
Comments Not Available
References
  • Rodriguez y Baena R, Gaetani P, Paoletti P: A study on cisternal CSF levels of arachidonic acid metabolites after aneurysmal subarachnoid hemorrhage. J Neurol Sci. 1988 Apr;84(2-3):329-35. [PubMed Link Image]
Biofluid CSF
Value 0.000153 +/- 1.711e-05 uM
Age Adult:>18 yrs old
Sex N/A
Comments Not Available
References
  • Nishisho T, Tonai T, Tamura Y, Ikata T: Experimental and clinical studies of eicosanoids in cerebrospinal fluid after spinal cord injury. Neurosurgery. 1996 Nov;39(5):950-6; discussion 956-7. [PubMed Link Image]
Associated Disorders
Condition References
Eczema
  • Hua Z, Fei H, Mingming X: Evaluation and interference of serum and skin lesion levels of leukotrienes in patients with eczema. Prostaglandins Leukot Essent Fatty Acids. 2006 Jul;75(1):51-5. Epub 2006 Jun 6. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Arachidonic Acid Metabolism SMP00075 Link Image map00590 Link Image
General References
  1. Sawazaki Y: [Leukotriene B4, leukotriene C4 and prostaglandin E2 in the serum, synovial fluid and synovium in patients with rheumatoid arthritis] Nippon Ika Daigaku Zasshi. 1989 Dec;56(6):559-64. [PubMed Link Image]
  2. Heimburger M, Palmblad JE: Effects of leukotriene C4 and D4, histamine and bradykinin on cytosolic calcium concentrations and adhesiveness of endothelial cells and neutrophils. Clin Exp Immunol. 1996 Mar;103(3):454-60. [PubMed Link Image]
  3. Lane SJ, Lee TH: Mast cell effector mechanisms. J Allergy Clin Immunol. 1996 Nov;98(5 Pt 2):S67-71; discussion S71-2. [PubMed Link Image]
  4. Romero R, Wu YK, Mazor M, Hobbins JC, Mitchell MD: Increased amniotic fluid leukotriene C4 concentration in term human parturition. Am J Obstet Gynecol. 1988 Sep;159(3):655-7. [PubMed Link Image]
  5. Paoletti P, Gaetani P, Grignani G, Pacchiarini L, Silvani V, Rodriguez y Baena R: CSF leukotriene C4 following subarachnoid hemorrhage. J Neurosurg. 1988 Oct;69(4):488-93. [PubMed Link Image]
  6. De Servi S, Ricevuti G, Mazzone A, Pasotti D, Bramucci E, Angoli L, Specchia G: Transcardiac release of leukotriene C4 by neutrophils in patients with coronary artery disease. J Am Coll Cardiol. 1991 Apr;17(5):1125-8. [PubMed Link Image]
  7. Koshino T, Takano S, Houjo T, Sano Y, Kudo K, Kihara H, Kitani S, Takaishi T, Hirai K, Ito K, Morita Y: Expression of 5-lipoxygenase and 5-lipoxygenase-activating protein mRNAs in the peripheral blood leukocytes of asthmatics. Biochem Biophys Res Commun. 1998 Jun 18;247(2):510-3. [PubMed Link Image]
  8. Richter L, Hesselbarth N, Eitner K, Schubert K, Bosseckert H, Krell H: Increased biliary secretion of cysteinyl-leukotrienes in human bile duct obstruction. J Hepatol. 1996 Nov;25(5):725-32. [PubMed Link Image]
  9. Sternfeld M, Fink A, Bentwich Z, Eliraz A: The role of acupuncture in asthma: changes in airways dynamics and LTC4 induced LAI. Am J Chin Med. 1989;17(3-4):129-34. [PubMed Link Image]
  10. Ponicke K, Forster W: Influence of leukotriene C4 on aggregation and on malondialdehyde formation of human blood platelets. Biomed Biochim Acta. 1984;43(8-9):S459-62. [PubMed Link Image]
  11. Chen ZS, Guo Y, Belinsky MG, Kotova E, Kruh GD: Transport of bile acids, sulfated steroids, estradiol 17-beta-D-glucuronide, and leukotriene C4 by human multidrug resistance protein 8 (ABCC11). Mol Pharmacol. 2005 Feb;67(2):545-57. Epub 2004 Nov 10. [PubMed Link Image]
  12. Sjolinder M, Tornhamre S, Claesson HE, Hydman J, Lindgren J: Characterization of a leukotriene C4 export mechanism in human platelets: possible involvement of multidrug resistance-associated protein 1. J Lipid Res. 1999 Mar;40(3):439-46. [PubMed Link Image]
  13. Angi MR, Bettero A, Filippi F, Salvalaio L, Benassi CA: [Quantitative evaluation of conjunctival irritation by simultaneous determination of histamine, serotonin and leukotriene C4 in tears] Ophtalmologie. 1987 Oct-Dec;1(4):509-11. [PubMed Link Image]
  14. Cruz JR, Cano F, Razin E, Acheson DW, Keusch GT: Fecal excretion of leukotriene C4 during human disease due to Shigella dysenteriae. J Pediatr Gastroenterol Nutr. 1995 Feb;20(2):179-83. [PubMed Link Image]
  15. Zijlstra FJ, Wilson JH: 15-HETE is the main eicosanoid present in mucus of ulcerative proctocolitis. Prostaglandins Leukot Essent Fatty Acids. 1991 May;43(1):55-9. [PubMed Link Image]
  16. Matsumoto S, Hayashi Y, Kinoshita I, Ikata T, Yamamoto S: Immunoaffinity purification of prostaglandin E2 and leukotriene C4 prior to radioimmunoassay: application to human synovial fluid. Ann Clin Biochem. 1993 Jan;30 ( Pt 1):60-8. [PubMed Link Image]
  17. Talbot SF, Atkins PC, Goetzl EJ, Zweiman B: Accumulation of leukotriene C4 and histamine in human allergic skin reactions. J Clin Invest. 1985 Aug;76(2):650-6. [PubMed Link Image]
  18. Kloprogge E, de Leeuw AJ, de Monchy JG, Kauffman HF: Cellular communication in leukotriene C4 production between eosinophils and neutrophils. Int Arch Allergy Appl Immunol. 1989;90(1):20-3. [PubMed Link Image]
  19. Damtew B, Spagnuolo PJ: Leukotriene C4 from vascular endothelium enhances neutrophil adhesiveness. Prostaglandins Leukot Essent Fatty Acids. 1997 Feb;56(2):111-6. [PubMed Link Image]
  20. Schauer U, Eckhart A, Muller R, Gemsa D, Rieger CH: Enhanced leukotriene C4 production by peripheral eosinophilic granulocytes from children with asthma. Int Arch Allergy Appl Immunol. 1989;90(3):201-6. [PubMed Link Image]
  21. Wikipedia Link Image
Metabolic Enzymes
  1. Gamma-glutamyltranspeptidase 1
  2. Leukotriene C4 synthase
  3. Multidrug resistance-associated protein 1
  4. Gamma-glutamyltransferase 6
  5. GGT7 protein
  6. Gamma-glutamyltransferase 5
Enzyme 1 [top]
Enzyme 1 ID 6005
Enzyme 1 Name Gamma-glutamyltranspeptidase 1
Enzyme 1 Synonyms
  1. GGT 1
  2. Gamma-glutamyltransferase 1
  3. CD224 antigen
  4. Gamma-glutamyltranspeptidase 1 heavy chain
  5. Gamma-glutamyltranspeptidase 1 light chain
Enzyme 1 Gene Name GGT1
Enzyme 1 Protein Sequence >Gamma-glutamyltranspeptidase 1 
MKKKLVVLGLLAVVLVLVIVGLCLWLPSASKEPDNHVYTRAAVAADAKQCSKIGRDALRD
GGSAVDAAIAALLCVGLMNAHSMGIGGGLFLTIYNSTTRKAEVINAREVAPRLAFATMFN
SSEQSQKGGLSVAVPGEIRGYELAHQRHGRLPWARLFQPSIQLARQGFPVGKGLAAALEN
KRTVIEQQPVLCEVFCRDRKVLREGERLTLPQLADTYETLAIEGAQAFYNGSLTAQIVKD
IQAAGGIVTAEDLNNYRAELIEHPLNISLGDVVLYMPSAPLSGPVLALILNILKGYNFSR
ESVESPEQKGLTYHRIVEAFRFAYAKRTLLGDPKFVDVTEVVRNMTSEFFAAQLRAQISD
DTTHPISYYKPEFYTPDDGGTAHLSVVAEDGSAVSATSTINLYFGSKVRSPVSGILFNNE
MDDFSSPSITNEFGVPPSPANFIQPGKQPLSSMCPTIMVGQDGQVRMVVGAAGGTQITTA
TALAIIYNLWFGYDVKRAVEEPRLHNQLLPNVTTVERNIDQAVTAALETRHHHTQIASTF
IAVVQAIVRTAGGWAAASDSRKGGEPAGY
Enzyme 1 Number of Residues 569
Enzyme 1 Molecular Weight 61409.7
Enzyme 1 Theoretical pI 7.14
Enzyme 1 GO Classification
Function
  • catalytic activity
  • gamma-glutamyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring amino-acyl groups
Process
—
Component
—
Enzyme 1 General Function Involved in gamma-glutamyltransferase activity
Enzyme 1 Specific Function Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracelular GSH level. It is part of the cell antioxidant defense mechanism. Catalyzes the transfer of the glutamyl moiety of glutathione to amino acids and dipeptide acceptors. Alternatively, glutathione can be hydrolyzed to give Cys-Gly and gamma glutamate. Isoform 3 seems to be inactive
Enzyme 1 Pathways
Enzyme 1 Reactions
  • (5-L-glutamyl)-peptide + an amino acid = peptide + 5-L-glutamyl amino acid [RN:R04159]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • 5-26
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 183138 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P19440 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name GGT1_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1710 bp 
ATGAAGAAGAAGTTAGTGGTGCTGGGCCTGCTGGCCGTGGTCCTGGTGCTGGTCATTGTC
GGCCTCTGTCTCTGGCTGCCCTCAGCCTCCAAGGAACCTGACAACCATGTGTACACCAGG
GCTGCCGTGGCCGCGGATGCCAAGCAGTGCTCGAAGATTGGGAGGGATGCACTGCGGGAC
GGTGGCTCTGCGGTGGATGCAGCCATTGCAGCCCTGTTGTGTGTGGGGCTCATGAATGCC
CACAGCATGGGCATCGGGGGTGGCCTCTTCCTCACCATCTACAACAGCACCACACGAAAA
GCTGAGGTCATCAACGCCCGCGAGGTGGCCCCCAGGCTGGCCTTTGCCACCATGTTCAAC
AGCTCGGAGCAGTCCCAGAAGGGGGGGCTGTCGGTGGCGGTGCCTGGGGAGATCCGAGGC
TATGAGCTGGCACACCAGCGGCATGGGCGGCTGCCCTGGGCTCGCCTCTTCCAGCCCAGC
ATCCAGCTGGCCCGCCAGGGCTTCCCCGTGGGCAAGGGCTTGGCGGCAGCCCTGGAAAAC
AAGCGGACCGTCATCGAGCAGCAGCCTGTCTTGTGTGAGGTGTTCTGCCGGGATAGAAAG
GTGCTTCGGGAGGGGGAGAGACTGACCCTGCCGCAGCTGGCTGACACCTACGAGACGCTG
GCCATCGAGGGTGCCCAGGCCTTCTACAACGGCAGCCTCACGGCCCAGATTGTGAAGGAC
ATCCAGGCGGCCGGGGGCATTGTGACAGCTGAGGACCTGAACAACTACCGTGCTGAGCTG
ATCGAGCACCCGCTGAACATCAGCCTGGGAGACGCGGTGCTGTACATGCCCAGTGCGCCG
CTCAGCGGGCCCGTGCTGGCCCTCATCCTCAACATCCTCAAAGGGTACAACTTCTCCCGG
GAGAGCGTGGAGAGCCCCGAGCAGAAGGGCCTGACGTACCACCGCATCGTAGAGGCTTTC
CGGTTTGCCTACGCCAAGAGGACCCTGCTTGGGGACCCCAAGTTTGTGGATGTGACTGAG
GTGGTCCGCAACATGACCTCCGAGTTCTTCGCTGCCCAGCTCCGGGCCCAGATCTCTGAC
GACACCACTCACCCGATCTCCTACTACAAGCCCGAGTTCTACACGCCGGATGACGGGGGC
ACTGCTCACCTGTCTGTCGTCGCAGAGGACGGCAGTGCTGTGTCCGCCACCAGCACCATC
AACCTCTACTTTGGCTCCAAGGTCCGCTCCCCGGTCAGCGGGATCCTGTTCAATAATGAA
ATGGACGACTTCAGCTCTCCCAGCATCACCAACGAGTTTGGGGTACCCCCCTCACCTGCC
AATTTCATCCAGCCAGGGAAGCAGCCGCTCTCGTCCATGTGCCCGACGATCATGGTGGGC
CAGGACGGCCAGGTCCGGATGGTGGTGGGAGCTGCTGGGGGCACACAGATCACCACGGCC
ACTGCACTGGCCATCATCTACAACCTCTGGTTCGGCTATGACGTGAAGCGGGCCGTGGAG
GAGCCCCGGCTGCACAACCAGCTTCTGCCCAACGTCACGACAGTGGAGAGAAACATTGAC
CAGGCAGTGACTGCAGCCCTGGAGACCCGGCACCATCACACCCAGATCGCGTCCACCTTC
ATCGCTGTGGTGCAAGCCATCGTCCGCACGGCTGGTGGCTGGGCAGCTGCCTCGGACTCC
AGGAAAGGCGGGGAGCCTGCCGGCTACTGA
Enzyme 1 GenBank Gene ID J04131 Link Image
Enzyme 1 GeneCard ID GGT1 Link Image
Enzyme 1 GenAtlas ID GGT1 Link Image
Enzyme 1 HGNC ID HGNC:4250 Link Image
Enzyme 1 Chromosome Location 2
Enzyme 1 Locus 22q11.23
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Rajpert-De Meyts E, Heisterkamp N, Groffen J: Cloning and nucleotide sequence of human gamma-glutamyl transpeptidase. Proc Natl Acad Sci U S A. 1988 Dec;85(23):8840-4. [PubMed Link Image]
  2. Sakamuro D, Yamazoe M, Matsuda Y, Kangawa K, Taniguchi N, Matsuo H, Yoshikawa H, Ogasawara N: The primary structure of human gamma-glutamyl transpeptidase. Gene. 1988 Dec 15;73(1):1-9. [PubMed Link Image]
  3. Pitot HC, Goodspeed D, Dunn T, Hendrich S, Maronpot RR, Moran S: Regulation of the expression of some genes for enzymes of glutathione metabolism in hepatotoxicity and hepatocarcinogenesis. Toxicol Appl Pharmacol. 1989 Jan;97(1):23-34. [PubMed Link Image]
  4. Goodspeed DC, Dunn TJ, Miller CD, Pitot HC: Human gamma-glutamyl transpeptidase cDNA: comparison of hepatoma and kidney mRNA in the human and rat. Gene. 1989 Mar 15;76(1):1-9. [PubMed Link Image]
  5. Pawlak A, Cohen EH, Octave JN, Schweickhardt R, Wu SJ, Bulle F, Chikhi N, Baik JH, Siegrist S, Guellaen G: An alternatively processed mRNA specific for gamma-glutamyl transpeptidase in human tissues. J Biol Chem. 1990 Feb 25;265(6):3256-62. [PubMed Link Image]
  6. Courtay C, Oster T, Michelet F, Visvikis A, Diederich M, Wellman M, Siest G: Gamma-glutamyltransferase: nucleotide sequence of the human pancreatic cDNA. Evidence for a ubiquitous gamma-glutamyltransferase polypeptide in human tissues. Biochem Pharmacol. 1992 Jun 23;43(12):2527-33. [PubMed Link Image]
  7. Wetmore LA, Gerard C, Drazen JM: Human lung expresses unique gamma-glutamyl transpeptidase transcripts. Proc Natl Acad Sci U S A. 1993 Aug 15;90(16):7461-5. [PubMed Link Image]
  8. Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [PubMed Link Image]
  9. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
  10. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  11. Tate SS, Khadse V, Wellner D: Renal gamma-glutamyl transpeptidases: structural and immunological studies. Arch Biochem Biophys. 1988 May 1;262(2):397-408. [PubMed Link Image]
  12. Chikhi N, Holic N, Guellaen G, Laperche Y: Gamma-glutamyl transpeptidase gene organization and expression: a comparative analysis in rat, mouse, pig and human species. Comp Biochem Physiol B Biochem Mol Biol. 1999 Apr;122(4):367-80. [PubMed Link Image]
  13. Tate SS, Ross ME: Human kidney gamma-glutamyl transpeptidase. Catalytic properties, subunit structure, and localization of the gamma-glutamyl binding site on the light subunit. J Biol Chem. 1977 Sep 10;252(17):6042-5. [PubMed Link Image]
  14. Tate SS, Galbraith RA: In vitro translation and processing of human hepatoma cell (Hep G2) gamma-glutamyl transpeptidase. Biochem Biophys Res Commun. 1988 Aug 15;154(3):1167-73. [PubMed Link Image]
  15. Ikeda Y, Fujii J, Taniguchi N: Significance of Arg-107 and Glu-108 in the catalytic mechanism of human gamma-glutamyl transpeptidase. Identification by site-directed mutagenesis. J Biol Chem. 1993 Feb 25;268(6):3980-5. [PubMed Link Image]
  16. Ikeda Y, Fujii J, Taniguchi N, Meister A: Human gamma-glutamyl transpeptidase mutants involving conserved aspartate residues and the unique cysteine residue of the light subunit. J Biol Chem. 1995 May 26;270(21):12471-5. [PubMed Link Image]
  17. Ikeda Y, Fujii J, Anderson ME, Taniguchi N, Meister A: Involvement of Ser-451 and Ser-452 in the catalysis of human gamma-glutamyl transpeptidase. J Biol Chem. 1995 Sep 22;270(38):22223-8. [PubMed Link Image]
  18. Ikeda Y, Fujii J, Taniguchi N: Effects of substitutions of the conserved histidine residues in human gamma-glutamyl transpeptidase. J Biochem (Tokyo). 1996 Jun;119(6):1166-70. [PubMed Link Image]
  19. Kristiansen TZ, Bunkenborg J, Gronborg M, Molina H, Thuluvath PJ, Argani P, Goggins MG, Maitra A, Pandey A: A proteomic analysis of human bile. Mol Cell Proteomics. 2004 Jul;3(7):715-28. Epub 2004 Apr 14. [PubMed Link Image]
  20. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
  21. Wollscheid B, Bausch-Fluck D, Henderson C, O'Brien R, Bibel M, Schiess R, Aebersold R, Watts JD: Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins. Nat Biotechnol. 2009 Apr;27(4):378-86. Epub 2009 Apr 6. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 6087
Enzyme 2 Name Leukotriene C4 synthase
Enzyme 2 Synonyms
  1. LTC4 synthase
  2. Leukotriene-C(4) synthase
Enzyme 2 Gene Name LTC4S
Enzyme 2 Protein Sequence >Leukotriene C4 synthase 
MKDEVALLAAVTLLGVLLQAYFSLQVISARRAFRVSPPLTTGPPEFERVYRAQVNCSEYF
PLFLATLWVAGIFFHEGAAALCGLVYLFARLRYFQGYARSAQLRLAPLYASARALWLLVA
LAALGLLAHFLPAALRAALLGRLRTLLPWA
Enzyme 2 Number of Residues 150
Enzyme 2 Molecular Weight 16566.5
Enzyme 2 Theoretical pI 10.40
Enzyme 2 GO Classification
Function
  • enzyme activator activity
  • enzyme regulator activity
Process
  • carboxylic acid metabolic process
  • cellular metabolic process
  • fatty acid metabolic process
  • icosanoid metabolic process
  • leukotriene metabolic process
  • metabolic process
  • monocarboxylic acid metabolic process
  • organic acid metabolic process
  • oxoacid metabolic process
  • unsaturated fatty acid metabolic process
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 2 General Function Involved in enzyme activator activity
Enzyme 2 Specific Function Catalyzes the conjugation of leukotriene A4 with reduced glutathione to form leukotriene C4
Enzyme 2 Pathways
Enzyme 2 Reactions
  • leukotriene C4 = leukotriene A4 + glutathione [RN:R03059]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • 7-27 49-69 74-94 105-124
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein Not Available
Enzyme 2 UniProtKB/Swiss-Prot ID Q16873 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name LTC4S_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >453 bp 
ATGAAGGACGAGGTAGCTCTACTGGCTGCTGTCACCCTCCTGGGAGTCCTGCTGCAAGCC
TACTTCTCCCTGCAGGTGATCTCGGCGCGCAGGGCCTTCCGCGTGTCGCCGCCGCTCACC
ACCGGCCCACCCGAGTTCGAGCGCGTCTACCGAGCCCAGGTGAACTGCAGCGAGTACTTC
CCGCTGTTCCTCGCCACGCTCTGGGTCGCCGGCATCTTCTTTCATGAAGGGGCGGCGGCC
CTGTGCGGCCTGGTCTACCTGTTCGCGCGCCTCCGCTACTTCCAGGGCTACGCGCGCTCC
GCGCAGCTCAGGCTGGCACCGCTGTACGCGAGCGCGCGCGCCCTCTGGCTGCTGGTGGCG
CTGGCTGCGCTCGGCCTGCTCGCCCACTTCCTCCCGGCCGCGCTGCGCGCCGCGCTCCTC
GGACGGCTCCGGACGCTGCTGCCGTGGGCCTGA
Enzyme 2 GenBank Gene ID U09353 Link Image
Enzyme 2 GeneCard ID LTC4S Link Image
Enzyme 2 GenAtlas ID LTC4S Link Image
Enzyme 2 HGNC ID HGNC:6719 Link Image
Enzyme 2 Chromosome Location 5
Enzyme 2 Locus 5q35
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Lam BK, Penrose JF, Freeman GJ, Austen KF: Expression cloning of a cDNA for human leukotriene C4 synthase, an integral membrane protein conjugating reduced glutathione to leukotriene A4. Proc Natl Acad Sci U S A. 1994 Aug 2;91(16):7663-7. [PubMed Link Image]
  2. Welsch DJ, Creely DP, Hauser SD, Mathis KJ, Krivi GG, Isakson PC: Molecular cloning and expression of human leukotriene-C4 synthase. Proc Natl Acad Sci U S A. 1994 Oct 11;91(21):9745-9. [PubMed Link Image]
  3. Penrose JF, Spector J, Baldasaro M, Xu K, Boyce J, Arm JP, Austen KF, Lam BK: Molecular cloning of the gene for human leukotriene C4 synthase. Organization, nucleotide sequence, and chromosomal localization to 5q35. J Biol Chem. 1996 May 10;271(19):11356-61. [PubMed Link Image]
  4. Bigby TD, Hodulik CR, Arden KC, Fu L: Molecular cloning of the human leukotriene C4 synthase gene and assignment to chromosome 5q35. Mol Med. 1996 Sep;2(5):637-46. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Nicholson DW, Ali A, Vaillancourt JP, Calaycay JR, Mumford RA, Zamboni RJ, Ford-Hutchinson AW: Purification to homogeneity and the N-terminal sequence of human leukotriene C4 synthase: a homodimeric glutathione S-transferase composed of 18-kDa subunits. Proc Natl Acad Sci U S A. 1993 Mar 1;90(5):2015-9. [PubMed Link Image]
  7. Penrose JF, Spector J, Lam BK, Friend DS, Xu K, Jack RM, Austen KF: Purification of human lung leukotriene C4 synthase and preparation of a polyclonal antibody. Am J Respir Crit Care Med. 1995 Jul;152(1):283-9. [PubMed Link Image]
  8. Goppelt-Struebe M: Two step purification of human and murine leukotriene C4 synthase. Biochim Biophys Acta. 1995 May 17;1256(2):257-61. [PubMed Link Image]
  9. Mayatepek E, Flock B: Leukotriene C4-synthesis deficiency: a new inborn error of metabolism linked to a fatal developmental syndrome. Lancet. 1998 Nov 7;352(9139):1514-7. [PubMed Link Image]
  10. Mayatepek E, Zelezny R, Lehmann WD, Hammond JW, Hoffmann GF: Defects in the synthesis of cysteinyl leukotrienes: a new group of inborn errors of metabolism. J Inherit Metab Dis. 2000 Jun;23(4):404-8. [PubMed Link Image]
  11. Christmas P, Weber BM, McKee M, Brown D, Soberman RJ: Membrane localization and topology of leukotriene C4 synthase. J Biol Chem. 2002 Aug 9;277(32):28902-8. Epub 2002 May 21. [PubMed Link Image]
  12. Strid T, Svartz J, Franck N, Hallin E, Ingelsson B, Soderstrom M, Hammarstrom S: Distinct parts of leukotriene C(4) synthase interact with 5-lipoxygenase and 5-lipoxygenase activating protein. Biochem Biophys Res Commun. 2009 Apr 17;381(4):518-22. Epub 2009 Feb 20. [PubMed Link Image]
  13. Ago H, Kanaoka Y, Irikura D, Lam BK, Shimamura T, Austen KF, Miyano M: Crystal structure of a human membrane protein involved in cysteinyl leukotriene biosynthesis. Nature. 2007 Aug 2;448(7153):609-12. Epub 2007 Jul 15. [PubMed Link Image]
  14. Martinez Molina D, Wetterholm A, Kohl A, McCarthy AA, Niegowski D, Ohlson E, Hammarberg T, Eshaghi S, Haeggstrom JZ, Nordlund P: Structural basis for synthesis of inflammatory mediators by human leukotriene C4 synthase. Nature. 2007 Aug 2;448(7153):613-6. Epub 2007 Jul 15. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 7252
Enzyme 3 Name Multidrug resistance-associated protein 1
Enzyme 3 Synonyms
  1. ATP-binding cassette sub-family C member 1
  2. Leukotriene C(4) transporter
  3. LTC4 transporter
Enzyme 3 Gene Name ABCC1
Enzyme 3 Protein Sequence >Multidrug resistance-associated protein 1 
MALRGFCSADGSDPLWDWNVTWNTSNPDFTKCFQNTVLVWVPCFYLWACFPFYFLYLSRH
DRGYIQMTPLNKTKTALGFLLWIVCWADLFYSFWERSRGIFLAPVFLVSPTLLGITMLLA
TFLIQLERRKGVQSSGIMLTFWLVALVCALAILRSKIMTALKEDAQVDLFRDITFYVYFS
LLLIQLVLSCFSDRSPLFSETIHDPNPCPESSASFLSRITFWWITGLIVRGYRQPLEGSD
LWSLNKEDTSEQVVPVLVKNWKKECAKTRKQPVKVVYSSKDPAQPKESSKVDANEEVEAL
IVKSPQKEWNPSLFKVLYKTFGPYFLMSFFFKAIHDLMMFSGPQILKLLIKFVNDTKAPD
WQGYFYTVLLFVTACLQTLVLHQYFHICFVSGMRIKTAVIGAVYRKALVITNSARKSSTV
GEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSVLAGVAVMVLMVPVN
AVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLK
KSAYLSAVGTFTWVCTPFLVALCTFAVYVTIDENNILDAQTAFVSLALFNILRFPLNILP
MVISSIVQASVSLKRLRIFLSHEELEPDSIERRPVKDGGGTNSITVRNATFTWARSDPPT
LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGSVAYVPQQAWIQND
SLRENILFGCQLEEPYYRSVIQACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLAR
AVYSNADIYLFDDPLSAVDAHVGKHIFENVIGPKGMLKNKTRILVTHSMSYLPQVDVIIV
MSGGKISEMGSYQELLARDGAFAEFLRTYASTEQEQDAEENGVTGVSGPGKEAKQMENGM
LVTDSAGKQLQRQLSSSSSYSGDISRHHNSTAELQKAEAKKEETWKLMEADKAQTGQVKL
SVYWDYMKAIGLFISFLSIFLFMCNHVSALASNYWLSLWTDDPIVNGTQEHTKVRLSVYG
ALGISQGIAVFGYSMAVSIGGILASRCLHVDLLHSILRSPMSFFERTPSGNLVNRFSKEL
DTVDSMIPEVIKMFMGSLFNVIGACIVILLATPIAAIIIPPLGLIYFFVQRFYVASSRQL
KRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLA
VRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVA
VERLKEYSETEKEAPWQIQETAPPSSWPQVGRVEFRNYCLRYREDLDFVLRHINVTINGG
EKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLF
SGSLRMNLDPFSQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCL
ARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVL
DKGEIQEYGAPSDLLQQRGLFYSMAKDAGLV
Enzyme 3 Number of Residues 1531
Enzyme 3 Molecular Weight 171589.5
Enzyme 3 Theoretical pI 7.11
Enzyme 3 GO Classification
Function
  • ATP binding
  • ATPase activity
  • ATPase activity, coupled to transmembrane movement of substances
  • P-P-bond-hydrolysis-driven transmembrane transporter activity
  • active transmembrane transporter activity
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • nucleoside binding
  • nucleoside-triphosphatase activity
  • nucleotide binding
  • primary active transmembrane transporter activity
  • purine nucleoside binding
  • pyrophosphatase activity
  • transmembrane transporter activity
  • transporter activity
Process
  • establishment of localization
  • transmembrane transport
  • transport
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 3 General Function Involved in ATP binding
Enzyme 3 Specific Function Mediates export of organic anions and drugs from the cytoplasm. Mediates ATP-dependent transport of glutathione and glutathione conjugates, leukotriene C4, estradiol-17-beta-o- glucuronide, methotrexate, antiviral drugs and other xenobiotics. Confers resistance to anticancer drugs. Hydrolyzes ATP with low efficiency
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • 34-54 75-95 101-121 134-154 173-193 317-337 364-384 441-461 465-485 548-568 591-611 968-988 1026-1046 1090-1110 1112-1132 1204-1224 1227-1247
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 134142337 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P33527 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name MRP1_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >4596 bp 
ATGGCGCTCCGGGGCTTCTGCAGCGCCGATGGCTCCGACCCGCTCTGGGACTGGAATGTC
ACGTGGAATACCAGCAACCCCGACTTCACCAAGTGCTTTCAGAACACGGTCCTCGTGTGG
GTGCCTTGTTTTTACCTCTGGGCCTGTTTCCCCTTCTACTTCCTCTATCTCTCCCGACAT
GACCGAGGCTACATTCAGATGACACCTCTCAACAAAACCAAAACTGCCTTGGGATTTTTG
CTGTGGATCGTCTGCTGGGCAGACCTCTTCTACTCTTTCTGGGAAAGAAGTCGGGGCATA
TTCCTGGCCCCAGTGTTTCTGGTCAGCCCAACTCTCTTGGGCATCACCATGCTGCTTGCT
ACCTTTTTAATTCAGCTGGAGAGGAGGAAGGGAGTTCAGTCTTCAGGGATCATGCTCACT
TTCTGGCTGGTAGCCCTAGTGTGTGCCCTAGCCATCCTGAGATCCAAAATTATGACAGCC
TTAAAAGAGGATGCCCAGGTGGACCTGTTTCGTGACATCACTTTCTACGTCTACTTTTCC
CTCTTACTCATTCAGCTCGTCTTGTCCTGTTTCTCAGATCGCTCACCCCTGTTCTCGGAA
ACCATCCACGACCCTAATCCCTGCCCAGAGTCCAGCGCTTCCTTCCTGTCGAGGATCACC
TTCTGGTGGATCACAGGGTTGATTGTCCGGGGCTACCGCCAGCCCCTGGAGGGCAGTGAC
CTCTGGTCCTTAAACAAGGAGGACACGTCGGAACAAGTCGTGCCTGTTTTGGTAAAGAAC
TGGAAGAAGGAATGCGCCAAGACTAGGAAGCAGCCGGTGAAGGTTGTGTACTCCTCCAAG
GATCCTGCCCAGCCGAAAGAGAGTTCCAAGGTGGATGCGAATGAGGAGGTGGAGGCTTTG
ATCGTCAAGTCCCCACAGAAGGAGTGGAACCCCTCTCTGTTTAAGGTGTTATACAAGACC
TTTGGGCCCTACTTCCTCATGAGCTTCTTCTTCAAGGCCATCCACGACCTGATGATGTTT
TCCGGGCCGCAGATCTTAAAGTTGCTCATCAAGTTCGTGAATGACACGAAGGCCCCAGAC
TGGCAGGGCTACTTCTACACCGTGCTGCTGTTTGTCACTGCCTGCCTGCAGACCCTCGTG
CTGCACCAGTACTTCCACATCTGCTTCGTCAGTGGCATGAGGATCAAGACCGCTGTCATT
GGGGCTGTCTATCGGAAGGCCCTGGTGATCACCAATTCAGCCAGAAAATCCTCCACGGTC
GGGGAGATTGTCAACCTCATGTCTGTGGACGCTCAGAGGTTCATGGACTTGGCCACGTAC
ATTAACATGATCTGGTCAGCCCCCCTGCAAGTCATCCTTGCTCTCTACCTCCTGTGGCTG
AATCTGGGCCCTTCCGTCCTGGCTGGAGTGGCGGTGATGGTCCTCATGGTGCCCGTCAAT
GCTGTGATGGCGATGAAGACCAAGACGTATCAGGTGGCCCACATGAAGAGCAAAGACAAT
CGGATCAAGCTGATGAACGAAATTCTCAATGGGATCAAAGTGCTAAAGCTTTATGCCTGG
GAGCTGGCATTCAAGGACAAGGTGCTGGCCATCAGGCAGGAGGAGCTGAAGGTGCTGAAG
AAGTCTGCCTACCTGTCAGCCGTGGGCACCTTCACCTGGGTCTGCACGCCCTTTCTGGTG
GCCTTGTGCACATTTGCCGTCTACGTGACCATTGACGAGAACAACATCCTGGATGCCCAG
ACAGCCTTCGTGTCTTTGGCCTTGTTCAACATCCTCCGGTTTCCCCTGAACATTCTCCCC
ATGGTCATCAGCAGCATCGTGCAGGCGAGTGTCTCCCTCAAACGCCTGAGGATCTTTCTC
TCCCATGAGGAGCTGGAACCTGACAGCATCGAGCGACGGCCTGTCAAAGACGGCGGGGGC
ACGAACAGCATCACCGTGAGGAATGCCACATTCACCTGGGCCAGGAGCGACCCTCCCACA
CTGAATGGCATCACCTTCTCCATCCCCGAAGGTGCTTTGGTGGCCGTGGTGGGCCAGGTG
GGCTGCGGAAAGTCGTCCCTGCTCTCAGCCCTCTTGGCTGAGATGGACAAAGTGGAGGGG
CACGTGGCTATCAAGGGCTCCGTGGCCTATGTGCCACAGCAGGCCTGGATTCAGAATGAT
TCTCTCCGAGAAAACATCCTTTTTGGATGTCAGCTGGAGGAACCATATTACAGGTCCGTG
ATACAGGCCTGTGCCCTCCTCCCAGACCTGGAAATCCTGCCCAGTGGGGATCGGACAGAG
ATTGGCGAGAAGGGCGTGAACCTGTCTGGGGGCCAGAAGCAGCGCGTGAGCCTGGCCCGG
GCCGTGTACTCCAACGCTGACATTTACCTCTTCGATGATCCCCTCTCAGCAGTGGATGCC
CATGTGGGAAAACACATCTTTGAAAATGTGATTGGCCCCAAGGGGATGCTGAAGAACAAG
ACGCGGATCTTGGTCACGCACAGCATGAGCTACTTGCCGCAGGTGGACGTCATCATCGTC
ATGAGTGGCGGCAAGATCTCTGAGATGGGCTCCTACCAGGAGCTGCTGGCTCGAGACGGC
GCCTTCGCTGAGTTCCTGCGTACCTATGCCAGCACAGAGCAGGAGCAGGATGCAGAGGAG
AACGGGGTCACGGGCGTCAGCGGTCCAGGGAAGGAAGCAAAGCAAATGGAGAATGGCATG
CTGGTGACGGACAGTGCAGGGAAGCAACTGCAGAGACAGCTCAGCAGCTCCTCCTCCTAT
AGTGGGGACATCAGCAGGCACCACAACAGCACCGCAGAACTGCAGAAAGCTGAGGCCAAG
AAGGAGGAGACCTGGAAGCTGATGGAGGCTGACAAGGCGCAGACAGGGCAGGTCAAGCTT
TCCGTGTACTGGGACTACATGAAGGCCATCGGACTCTTCATCTCCTTCCTCAGCATCTTC
CTTTTCATGTGTAACCATGTGTCCGCGCTGGCTTCCAACTATTGGCTCAGCCTCTGGACT
GATGACCCCATCGTCAACGGGACTCAGGAGCACACGAAAGTCCGGCTGAGCGTCTATGGA
GCCCTGGGCATTTCACAAGGGATCGCCGTGTTTGGCTACTCCATGGCCGTGTCCATCGGG
GGGATCTTGGCTTCCCGCTGTCTGCACGTGGACCTGCTGCACAGCATCCTGCGGTCACCC
ATGAGCTTCTTTGAGCGGACCCCCAGTGGGAACCTGGTGAACCGCTTCTCCAAGGAGCTG
GACACAGTGGACTCCATGATCCCGGAGGTCATCAAGATGTTCATGGGCTCCCTGTTCAAC
GTCATTGGTGCCTGCATCGTTATCCTGCTGGCCACGCCCATCGCCGCCATCATCATCCCG
CCCCTTGGCCTCATCTACTTCTTCGTCCAGAGGTTCTACGTGGCTTCCTCCCGGCAGCTG
AAGCGCCTCGAGTCGGTCAGCCGCTCCCCGGTCTATTCCCATTTCAACGAGACCTTGCTG
GGGGTCAGCGTCATTCGAGCCTTCGAGGAGCAGGAGCGCTTCATCCACCAGAGTGACCTG
AAGGTGGACGAGAACCAGAAGGCCTATTACCCCAGCATCGTGGCCAACAGGTGGCTGGCC
GTGCGGCTGGAGTGTGTGGGCAACTGCATCGTTCTGTTTGCTGCCCTGTTTGCGGTGATC
TCCAGGCACAGCCTCAGTGCTGGCTTGGTGGGCCTCTCAGTGTCTTACTCATTGCAGGTC
ACCACGTACTTGAACTGGCTGGTTCGGATGTCATCTGAAATGGAAACCAACATCGTGGCC
GTGGAGAGGCTCAAGGAGTATTCAGAGACTGAGAAGGAGGCGCCCTGGCAAATCCAGGAG
ACAGCTCCGCCCAGCAGCTGGCCCCAGGTGGGCCGAGTGGAATTCCGGAACTACTGCCTG
CGCTACCGAGAGGACCTGGACTTCGTTCTCAGGCACATCAATGTCACGATCAATGGGGGA
GAAAAGGTCGGCATCGTGGGGCGGACGGGAGCTGGGAAGTCGTCCCTGACCCTGGGCTTA
TTTCGGATCAACGAGTCTGCCGAAGGAGAGATCATCATCGATGGCATCAACATCGCCAAG
ATCGGCCTGCACGACCTCCGCTTCAAGATCACCATCATCCCCCAGGACCCTGTTTTGTTT
TCGGGTTCCCTCCGAATGAACCTGGACCCATTCAGCCAGTACTCGGATGAAGAAGTCTGG
ACGTCCCTGGAGCTGGCCCACCTGAAGGACTTCGTGTCAGCCCTTCCTGACAAGCTAGAC
CATGAATGTGCAGAAGGCGGGGAGAACCTCAGTGTCGGGCAGCGCCAGCTTGTGTGCCTA
GCCCGGGCCCTGCTGAGGAAGACGAAGATCCTTGTGTTGGATGAGGCCACGGCAGCCGTG
GACCTGGAAACGGACGACCTCATCCAGTCCACCATCCGGACACAGTTCGAGGACTGCACC
GTCCTCACCATCGCCCACCGGCTCAACACCATCATGGACTACACAAGGGTGATCGTCTTG
GACAAAGGAGAAATCCAGGAGTACGGCGCCCCATCGGACCTCCTGCAGCAGAGAGGTCTT
TTCTACAGCATGGCCAAAGACGCCGGCTTGGTGTGA
Enzyme 3 GenBank Gene ID NM_004996.3 Link Image
Enzyme 3 GeneCard ID ABCC1 Link Image
Enzyme 3 GenAtlas ID ABCC1 Link Image
Enzyme 3 HGNC ID HGNC:51 Link Image
Enzyme 3 Chromosome Location 1
Enzyme 3 Locus 16p13.1
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Cole SP, Bhardwaj G, Gerlach JH, Mackie JE, Grant CE, Almquist KC, Stewart AJ, Kurz EU, Duncan AM, Deeley RG: Overexpression of a transporter gene in a multidrug-resistant human lung cancer cell line. Science. 1992 Dec 4;258(5088):1650-4. [PubMed Link Image]
  2. Cole SP, Deeley RG: Multidrug resistance-associated protein: sequence correction. Science. 1993 May 14;260(5110):879. [PubMed Link Image]
  3. Grant CE, Kurz EU, Cole SP, Deeley RG: Analysis of the intron-exon organization of the human multidrug-resistance protein gene (MRP) and alternative splicing of its mRNA. Genomics. 1997 Oct 15;45(2):368-78. [PubMed Link Image]
  4. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed Link Image]
  5. Loftus BJ, Kim UJ, Sneddon VP, Kalush F, Brandon R, Fuhrmann J, Mason T, Crosby ML, Barnstead M, Cronin L, Deslattes Mays A, Cao Y, Xu RX, Kang HL, Mitchell S, Eichler EE, Harris PC, Venter JC, Adams MD: Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q. Genomics. 1999 Sep 15;60(3):295-308. [PubMed Link Image]
  6. Hipfner DR, Almquist KC, Leslie EM, Gerlach JH, Grant CE, Deeley RG, Cole SP: Membrane topology of the multidrug resistance protein (MRP). A study of glycosylation-site mutants reveals an extracytosolic NH2 terminus. J Biol Chem. 1997 Sep 19;272(38):23623-30. [PubMed Link Image]
  7. Kast C, Gros P: Topology mapping of the amino-terminal half of multidrug resistance-associated protein by epitope insertion and immunofluorescence. J Biol Chem. 1997 Oct 17;272(42):26479-87. [PubMed Link Image]
  8. Kast C, Gros P: Epitope insertion favors a six transmembrane domain model for the carboxy-terminal portion of the multidrug resistance-associated protein. Biochemistry. 1998 Feb 24;37(8):2305-13. [PubMed Link Image]
  9. Sjolinder M, Tornhamre S, Claesson HE, Hydman J, Lindgren J: Characterization of a leukotriene C4 export mechanism in human platelets: possible involvement of multidrug resistance-associated protein 1. J Lipid Res. 1999 Mar;40(3):439-46. [PubMed Link Image]
  10. Robbiani DF, Finch RA, Jager D, Muller WA, Sartorelli AC, Randolph GJ: The leukotriene C(4) transporter MRP1 regulates CCL19 (MIP-3beta, ELC)-dependent mobilization of dendritic cells to lymph nodes. Cell. 2000 Nov 22;103(5):757-68. [PubMed Link Image]
  11. Cui L, Hou YX, Riordan JR, Chang XB: Mutations of the Walker B motif in the first nucleotide binding domain of multidrug resistance protein MRP1 prevent conformational maturation. Arch Biochem Biophys. 2001 Aug 1;392(1):153-61. [PubMed Link Image]
  12. Ito K, Olsen SL, Qiu W, Deeley RG, Cole SP: Mutation of a single conserved tryptophan in multidrug resistance protein 1 (MRP1/ABCC1) results in loss of drug resistance and selective loss of organic anion transport. J Biol Chem. 2001 May 11;276(19):15616-24. Epub 2001 Feb 21. [PubMed Link Image]
  13. Zhang DW, Cole SP, Deeley RG: Identification of an amino acid residue in multidrug resistance protein 1 critical for conferring resistance to anthracyclines. J Biol Chem. 2001 Apr 20;276(16):13231-9. Epub 2001 Jan 23. [PubMed Link Image]
  14. Situ D, Haimeur A, Conseil G, Sparks KE, Zhang D, Deeley RG, Cole SP: Mutational analysis of ionizable residues proximal to the cytoplasmic interface of membrane spanning domain 3 of the multidrug resistance protein, MRP1 (ABCC1): glutamate 1204 is important for both the expression and catalytic activity of the transporter. J Biol Chem. 2004 Sep 10;279(37):38871-80. Epub 2004 Jun 18. [PubMed Link Image]
  15. Zhang DW, Nunoya K, Vasa M, Gu HM, Theis A, Cole SP, Deeley RG: Transmembrane helix 11 of multidrug resistance protein 1 (MRP1/ABCC1): identification of polar amino acids important for substrate specificity and binding of ATP at nucleotide binding domain 1. Biochemistry. 2004 Jul 27;43(29):9413-25. [PubMed Link Image]
  16. Conseil G, Deeley RG, Cole SP: Functional importance of three basic residues clustered at the cytosolic interface of transmembrane helix 15 in the multidrug and organic anion transporter MRP1 (ABCC1). J Biol Chem. 2006 Jan 6;281(1):43-50. Epub 2005 Oct 17. [PubMed Link Image]
  17. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  18. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  19. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  20. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  21. Ramaen O, Leulliot N, Sizun C, Ulryck N, Pamlard O, Lallemand JY, Tilbeurgh H, Jacquet E: Structure of the human multidrug resistance protein 1 nucleotide binding domain 1 bound to Mg2+/ATP reveals a non-productive catalytic site. J Mol Biol. 2006 Jun 16;359(4):940-9. Epub 2006 May 2. [PubMed Link Image]
  22. Le Saux O, Urban Z, Tschuch C, Csiszar K, Bacchelli B, Quaglino D, Pasquali-Ronchetti I, Pope FM, Richards A, Terry S, Bercovitch L, de Paepe A, Boyd CD: Mutations in a gene encoding an ABC transporter cause pseudoxanthoma elasticum. Nat Genet. 2000 Jun;25(2):223-7. [PubMed Link Image]
  23. Ringpfeil F, Lebwohl MG, Christiano AM, Uitto J: Pseudoxanthoma elasticum: mutations in the MRP6 gene encoding a transmembrane ATP-binding cassette (ABC) transporter. Proc Natl Acad Sci U S A. 2000 May 23;97(11):6001-6. [PubMed Link Image]
  24. Conrad S, Kauffmann HM, Ito K, Deeley RG, Cole SP, Schrenk D: Identification of human multidrug resistance protein 1 (MRP1) mutations and characterization of a G671V substitution. J Hum Genet. 2001;46(11):656-63. [PubMed Link Image]
  25. Perdu J, Germain DP: Identification of novel polymorphisms in the pM5 and MRP1 (ABCC1) genes at locus 16p13.1 and exclusion of both genes as responsible for pseudoxanthoma elasticum. Hum Mutat. 2001;17(1):74-5. [PubMed Link Image]
  26. Ito S, Ieiri I, Tanabe M, Suzuki A, Higuchi S, Otsubo K: Polymorphism of the ABC transporter genes, MDR1, MRP1 and MRP2/cMOAT, in healthy Japanese subjects. Pharmacogenetics. 2001 Mar;11(2):175-84. [PubMed Link Image]
  27. Ley TJ, Mardis ER, Ding L, Fulton B, McLellan MD, Chen K, Dooling D, Dunford-Shore BH, McGrath S, Hickenbotham M, Cook L, Abbott R, Larson DE, Koboldt DC, Pohl C, Smith S, Hawkins A, Abbott S, Locke D, Hillier LW, Miner T, Fulton L, Magrini V, Wylie T, Glasscock J, Conyers J, Sander N, Shi X, Osborne JR, Minx P, Gordon D, Chinwalla A, Zhao Y, Ries RE, Payton JE, Westervelt P, Tomasson MH, Watson M, Baty J, Ivanovich J, Heath S, Shannon WD, Nagarajan R, Walter MJ, Link DC, Graubert TA, DiPersio JF, Wilson RK: DNA sequencing of a cytogenetically normal acute myeloid leukaemia genome. Nature. 2008 Nov 6;456(7218):66-72. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 12987
Enzyme 4 Name Gamma-glutamyltransferase 6
Enzyme 4 Synonyms
  1. GGT 6
  2. Gamma-glutamyltranspeptidase 6
  3. Gamma-glutamyltransferase 6 heavy chain
  4. Gamma-glutamyltransferase 6 light chain
Enzyme 4 Gene Name GGT6
Enzyme 4 Protein Sequence >Gamma-glutamyltransferase 6 
MERAEEPVVYQKLLPWEPSLESEEEVEEEETSEALVLNPRRHQDSSRNKAGGLPGTWARV
VAALLLLAVGCSLAVRQLQNQGRSTGSLGSVAPPPGGHSHGPGVYHHGAIISPAGRELLV
AGGNVVDAGVGAALCLAVVHPHATGLGAMFWGLFHDSSSGNSTALTSGPAQTLAPGLGLP
AALPTLHLLHARFGRLPWPRLLVGPTTLAQEGFLVDTPLARALVARGTEGLCPLLCHADG
TPLGAGARATNPQLAAVLRSAALAPTSDLAGDALLSLLAGDLGVEVPSAVPRPTLEPAEQ
LPVPQGILFTTPSPSAGPELLALLEAALRSGAPIPDPCPPFLQTAVSPESSALAAVDSSG
SVLLLTSSLNCSFGSAHLSPSTGVLLSNLVAKSTTSAWACPLILRGSLDDTEADVLGLVA
SGTPDVARAMTHTLLRHLAARPPTQAQHQHQGQQEPTEHPSTCGQGTLLQVAAHTEHAHV
SSVPHACCPFQGF
Enzyme 4 Number of Residues 493
Enzyme 4 Molecular Weight 50508.8
Enzyme 4 Theoretical pI 6.04
Enzyme 4 GO Classification
Function
  • catalytic activity
  • gamma-glutamyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring amino-acyl groups
Process
—
Component
—
Enzyme 4 General Function Involved in gamma-glutamyltransferase activity
Enzyme 4 Specific Function Cleaves glutathione conjugates
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions
  • (5-L-glutamyl)-peptide + an amino acid = peptide + 5-L-glutamyl amino acid [RN:R04159]
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • 55-75
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 171543825 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q6P531 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name GGT6_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1482 bp 
ATGGAGCGGGCAGAAGAGCCCGTGGTCTATCAGAAGCTGCTGCCCTGGGAGCCAAGCTTG
GAGTCGGAGGAGGAAGTGGAGGAGGAGGAGACATCAGAGGCGCTGGTTCTAAACCCCCGG
AGGCACCAGGACTCTTCCAGGAACAAGGCTGGCGGGCTGCCCGGAACCTGGGCCCGTGTA
GTGGCAGCCCTGCTGCTGCTGGCTGTTGGCTGCTCCCTGGCTGTGAGGCAGCTCCAGAAT
CAGGGCAGGTCGACAGGAAGCTTGGGCTCTGTGGCCCCTCCACCCGGCGGACACTCCCAC
GGCCCTGGCGTATACCACCACGGTGCCATCATCAGCCCTGCAGGCCGAGAGCTGCTTGTT
GCCGGGGGCAACGTCGTGGATGCTGGAGTTGGAGCTGCATTGTGCCTGGCAGTGGTGCAT
CCTCATGCCACGGGGCTAGGTGCCATGTTTTGGGGCCTCTTCCACGATAGCTCCTCAGGC
AATTCCACGGCCCTGACATCAGGCCCAGCACAGACCCTGGCCCCCGGCCTGGGGCTGCCC
GCGGCTCTGCCCACCCTGCACCTGCTGCATGCACGCTTCGGCCGCCTGCCCTGGCCACGC
CTGCTAGTGGGCCCCACCACGCTGGCTCAGGAGGGCTTCCTGGTGGACACACCCCTGGCA
AGGGCTCTGGTGGCTCGGGGCACAGAAGGCCTCTGTCCACTACTTTGCCATGCTGATGGG
ACACCCCTGGGCGCTGGGGCCCGAGCCACCAACCCACAACTGGCAGCTGTGCTTCGCAGC
GCAGCCCTCGCTCCCACCTCAGACCTTGCTGGGGATGCTCTACTGAGTCTACTGGCGGGA
GACCTGGGGGTGGAGGTGCCCTCGGCTGTGCCCAGGCCCACTTTGGAACCAGCAGAGCAG
CTACCTGTGCCCCAGGGCATCCTGTTCACCACCCCCAGTCCCTCAGCTGGCCCAGAACTG
CTGGCACTGTTGGAGGCAGCCCTGCGCTCCGGGGCGCCCATCCCTGACCCCTGCCCACCG
TTCCTGCAGACTGCTGTGAGCCCCGAGAGCAGTGCCCTGGCCGCCGTGGACAGCAGCGGC
TCTGTGCTCCTTCTCACCTCCTCGCTCAACTGCTCCTTTGGCTCTGCACACCTGTCCCCA
AGCACTGGGGTTCTGCTCAGCAACCTGGTGGCCAAGTCTACCACTAGTGCCTGGGCCTGC
CCCCTCATCCTCCGTGGCAGCCTGGATGACACAGAGGCTGATGTGTTGGGGCTTGTGGCT
TCAGGGACCCCTGATGTGGCCAGGGCCATGACTCACACCCTACTCAGGCATCTGGCAGCA
AGGCCCCCTACCCAGGCCCAGCACCAGCATCAGGGTCAGCAAGAACCAACAGAGCATCCC
AGCACTTGTGGCCAAGGGACCCTGCTCCAGGTGGCAGCCCACACAGAGCACGCCCATGTC
TCCAGTGTCCCCCATGCCTGCTGCCCCTTCCAGGGGTTCTAA
Enzyme 4 GenBank Gene ID NM_001122890.1 Link Image
Enzyme 4 GeneCard ID GGT6 Link Image
Enzyme 4 GenAtlas ID GGT6 Link Image
Enzyme 4 HGNC ID HGNC:26891 Link Image
Enzyme 4 Chromosome Location 1
Enzyme 4 Locus 17p13.2
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Heisterkamp N, Groffen J, Warburton D, Sneddon TP: The human gamma-glutamyltransferase gene family. Hum Genet. 2008 May;123(4):321-32. Epub 2008 Mar 21. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 15189
Enzyme 5 Name GGT7 protein
Enzyme 5 Synonyms Not Available
Enzyme 5 Gene Name GGT7
Enzyme 5 Protein Sequence >GGT7 protein 
MAAENEASQESALGAYSPVDYMSITSFPRLPEDEPAPAAPLRGRKDEDAFLGDPDTDPDS
FLKSARLQRLPSSSSEMGSQDGSPLRETRKDPFSAAAAECSCRQDGLTVIVTACLTFATG
VTVALVMQIYFGDPQIFQQGAVVTDAARCTSLGIEVLSKQGSSVDAAVAAALCLGIVAPH
SSGLGGGGVMLVHDIRRNESHLIDFRESAPGALREETLQRSWETKPGLLVGVPGMVKGLH
EAHQLYGRLPWSQVLAFAAAVAQDGFNVTHDLARALAEQLPPNMSERFRETFLPSGRPPL
PGSLLHRPDLAEVLDVLGTSGPAAFYAGGNLTLEMVAEAQHAGGVITEEDFSNYSALVEK
PVCGVYRGHLVLSPPPPHTGPALISALNILEGFNLTSLVSREQALHWVAETLKIALALAS
RLGDPVYDSTITESMDDMLSKVEAAYLRGHINDSQAAPAPLLPVYELDGAPTAAQVLIMG
PDDFIVAMVSSLNQPFGSGLITPSGILLNSQMLDFSWPNRTANHSAPSLENSVQPGKRPL
SFLLPTVVRPAEGLCGTYLALGANGAARGLSGLTQVLLNVLTLNRNLSDSLA
Enzyme 5 Number of Residues 592
Enzyme 5 Molecular Weight 62565.3
Enzyme 5 Theoretical pI 4.64
Enzyme 5 GO Classification
Function
  • catalytic activity
  • gamma-glutamyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring amino-acyl groups
Process
—
Component
—
Enzyme 5 General Function Involved in gamma-glutamyltransferase activity
Enzyme 5 Specific Function Not Available
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 118600847 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID A0PJJ9 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name A0PJJ9_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1777 bp 
ATGGCGGCGGAGAACGAGGCCAGCCAGGAGAGCGCCCTGGGCGCCTACTCGCCAGTGGAC
TACATGAGCATCACCAGCTTCCCGCGGCTGCCCGAGGACGAGCCGGCGCCCGCGGCCCCG
CTGAGGGGCCGCAAGGACGAGGACGCCTTTCTGGGAGACCCCGACACCGACCCGGACTCC
TTCCTGAAGTCTGCACGGCTGCAGCGGCTGCCATCGTCGTCGTCGGAGATGGGCAGCCAA
GACGGGTCGCCGCTACGCGAGACGCGCAAAGACCCGTTCTCCGCCGCAGCGGCCGAGTGC
TCCTGCCGCCAGGATGGGCTCACGGTCATCGTCACGGCCTGTCTCACCTTCGCTACCGGT
GTCACCGTGGCGCTGGTCATGCAGATCTACTTCGGGGACCCCCAGATCTTCCAGCAGGGT
GCCGTGGTGACCGATGCTGCCCGCTGCACTTCACTGGGCATCGAGGTGCTCAGTAAACAG
GGATCTTCTGTGGACGCAGCGGTGGCAGCAGCCTTGTGTTTGGGTATCGTGGCTCCACAC
AGTTCTGGCCTGGGCGGTGGGGGCGTGATGCTGGTACATGACATCCGACGAAATGAGAGC
CACCTAATTGATTTCCGGGAGTCCGCACCAGGGGCCCTCAGGGAAGAGACCCTGCAAAGA
TCCTGGGAGACCAAGCCTGGGCTCTTGGTGGGGGTTCCCGGAATGGTGAAAGGGCTACAT
GAAGCTCACCAGCTCTATGGCAGGCTGCCATGGTCCCAAGTCCTGGCCTTTGCAGCAGCT
GTGGCCCAAGATGGCTTCAACGTGACTCATGATCTAGCCCGTGCCCTGGCTGAACAGCTG
CCACCCAACATGTCCGAGCGCTTCCGGGAGACGTTCCTGCCATCGGGCCGCCCGCCACTA
CCTGGCTCGTTGCTGCATCGGCCCGACCTGGCTGAGGTGCTGGATGTACTTGGCACCTCC
GGCCCGGCTGCCTTCTACGCAGGTGGCAACCTCACACTGGAGATGGTGGCCGAGGCTCAG
CACGCAGGGGGTGTCATAACCGAAGAGGACTTCAGCAATTACAGCGCCCTTGTGGAGAAG
CCTGTGTGTGGCGTGTACAGAGGCCACCTGGTTCTTAGTCCCCCACCTCCGCACACGGGC
CCTGCCCTCATCAGTGCTCTCAACATCCTGGAGGGCTTCAATCTCACCAGCCTGGTATCC
CGAGAACAGGCTCTTCACTGGGTGGCAGAGACCCTGAAGATTGCATTAGCCCTGGCCAGC
AGACTGGGAGATCCCGTCTATGATTCTACCATCACTGAGAGCATGGATGACATGCTCAGC
AAGGTGGAGGCCGCCTACCTCCGGGGCCATATCAATGACTCCCAGGCAGCCCCTGCCCCA
CTCCTGCCTGTCTATGAACTAGACGGAGCTCCCACGGCTGCCCAGGTGCTGATCATGGGA
CCTGATGACTTCATTGTGGCCATGGTTAGCTCCCTGAACCAGCCCTTTGGCAGCGGCCTT
ATCACCCCCTCGGGGATCCTGCTCAACAGCCAGATGCTGGACTTCTCCTGGCCCAACCGG
ACAGCTAACCACTCTGCACCCAGCCTGGAGAATTCAGTGCAGCCAGGGAAGCGGCCACTC
TCTTTCCTGCTGCCCACAGTGGTCCGACCCGCGGAGGGGCTCTGTGGAACCTACCTCGCT
CTGGGGGCCAATGGAGCTGCGCGGGGCCTCAGCGGCCTGACACAGGTTCTGCTGAATGTC
CTGACCTTGAACCGGAACCTGAGTGACAGCCTGGCCC
Enzyme 5 GenBank Gene ID BC033745 Link Image
Enzyme 5 GeneCard ID GGT7 Link Image
Enzyme 5 GenAtlas ID GGT7 Link Image
Enzyme 5 HGNC ID HGNC:4259 Link Image
Enzyme 5 Chromosome Location 2
Enzyme 5 Locus 20q11.22
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 15190
Enzyme 6 Name Gamma-glutamyltransferase 5
Enzyme 6 Synonyms Not Available
Enzyme 6 Gene Name GGT5
Enzyme 6 Protein Sequence >Gamma-glutamyltransferase 5 
MARGYGATVSLVLLGLGLALAVIVLAVVLSRHQAPCGPQAFAHAAVAADSKVCSDIGRAI
LQQQGSPVDATIAALVCTSVVNPQSMGLGGGVIFTIYNVTTGKVEVINARETVPASHAPS
LLDQCAQALPLGTGAQWIGVPGELRGYAEAHRRHGRLPWAQLFQPTIALLRGGHVVAPVL
SRFLHNSILRPSLQASTLRQLFFNGTEPLRPQDPLPWPALATTLETVATEGVEVFYTGRL
GQMLVEDIAKEGSQLTLQDLAKFQPEVVDALEVPLGDYTLYSPPPPAGGAILSFILNVLR
GFNFSTESMARPEGRVNVYHHLVETLKFAKGQRWRLGDPRSHPKLQNASRDLLGETLAQL
IRQQIDGRGDHQLSHYSLAEAWGHGTGTSHVSVLGEDGSAVAATSTINTPFGAMVYSPRT
GIILNNELLDLCERCPRGSGTTPSPAVSGDRVGGAPGRCWPPVPGERSPSSMVPSILINK
AQGSKLVIGGAGGELIISAVAQAIMSKLWLGFDLRAAIAAPILHVNSKGCVEYEPNFSQE
VQRGLQDRGQNQTQRPFFLNVVQAVSQEGACVYAVSDLRKSGEAAGY
Enzyme 6 Number of Residues 587
Enzyme 6 Molecular Weight 62331.8
Enzyme 6 Theoretical pI 7.59
Enzyme 6 GO Classification
Function
  • catalytic activity
  • gamma-glutamyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring amino-acyl groups
Process
—
Component
—
Enzyme 6 General Function Involved in gamma-glutamyltransferase activity
Enzyme 6 Specific Function Not Available
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 49256405 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q6GMP0 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name Q6GMP0_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1764 bp 
ATGGCCCGGGGCTACGGGGCCACGGTCAGCCTAGTCCTGCTGGGTCTGGGGCTGGCGCTG
GCTGTCATTGTGCTGGCTGTGGTCCTCTCTCGACACCAGGCCCCATGTGGCCCCCAGGCC
TTTGCCCACGCTGCTGTTGCCGCCGACTCCAAGGTCTGCTCGGATATTGGACGAGCCATC
CTCCAGCAGCAGGGCTCACCCGTGGATGCCACCATCGCGGCTCTGGTCTGCACCAGCGTC
GTCAACCCTCAGAGCATGGGCCTGGGCGGAGGGGTCATCTTCACCATCTACAATGTGACA
ACAGGGAAGGTGGAGGTCATCAATGCCCGGGAGACGGTGCCGGCCAGCCACGCCCCGAGC
CTGCTGGACCAGTGTGCACAGGCTCTGCCACTGGGCACAGGGGCCCAGTGGATCGGGGTG
CCCGGGGAGCTCCGTGGCTATGCCGAGGCCCACCGCCGCCATGGCCGCCTGCCCTGGGCG
CAGCTGTTCCAGCCCACCATCGCGCTGCTCCGAGGGGGGCATGTGGTGGCCCCTGTCCTC
AGCCGTTTCCTGCACAACAGCATCCTGCGGCCTTCCTTGCAGGCGTCAACCCTGCGCCAG
CTCTTCTTCAACGGGACAGAACCCCTGAGGCCTCAGGACCCACTCCCATGGCCTGCACTG
GCCACCACCCTGGAGACCGTGGCCACAGAGGGCGTGGAGGTCTTCTACACGGGGAGGCTG
GGCCAGATGCTGGTGGAGGACATTGCCAAGGAAGGGAGCCAGCTGACGCTGCAGGACCTG
GCCAAGTTCCAGCCCGAGGTGGTGGATGCCCTGGAGGTGCCCCTGGGGGACTATACCCTG
TACTCACCACCGCCGCCTGCAGGGGGTGCCATTCTCAGCTTTATCCTCAACGTGCTAAGA
GGGTTCAACTTCTCAACAGAGTCTATGGCCAGGCCTGAAGGGAGGGTGAACGTGTACCAC
CACCTTGTAGAGACGCTCAAGTTTGCCAAGGGGCAGAGGTGGAGGCTGGGGGACCCTCGA
AGCCACCCGAAGCTCCAGAATGCCTCCCGGGACCTGCTGGGGGAGACCCTGGCCCAGCTC
ATCCGCCAACAGATCGATGGCCGGGGGGACCACCAGCTCAGCCACTACAGCTTGGCCGAG
GCCTGGGGCCACGGGACAGGCACGTCCCATGTGTCTGTGCTGGGGGAGGATGGCAGCGCC
GTGGCTGCCACCAGCACCATCAACACACCCTTTGGAGCGATGGTGTATTCACCACGGACA
GGCATCATCCTCAACAACGAGCTCCTGGACTTATGCGAGCGATGCCCCCGGGGTTCCGGC
ACCACCCCCTCACCTGCAGTGAGTGGAGACAGGGTGGGTGGAGCTCCCGGAAGGTGCTGG
CCCCCAGTTCCAGGCGAGCGTTCCCCATCCTCCATGGTGCCCTCCATCTTGATCAACAAA
GCCCAGGGGTCGAAGCTAGTGATTGGCGGGGCTGGCGGGGAGCTCATCATCTCTGCTGTG
GCCCAGGCCATCATGAGCAAGCTGTGGCTTGGCTTTGACCTGAGAGCGGCCATTGCAGCC
CCCATCCTGCATGTCAACAGCAAGGGCTGTGTGGAGTACGAGCCCAACTTCAGCCAGGAG
GTGCAGAGGGGACTCCAAGACCGTGGCCAGAACCAGACCCAGAGGCCCTTCTTCCTGAAC
GTGGTCCAGGCTGTGTCCCAGGAGGGGGCCTGTGTGTACGCCGTCTCGGACCTGAGGAAG
AGTGGGGAGGCCGCAGGCTACTAA
Enzyme 6 GenBank Gene ID BC073999 Link Image
Enzyme 6 GeneCard ID GGT5 Link Image
Enzyme 6 GenAtlas ID GGT5 Link Image
Enzyme 6 HGNC ID HGNC:4260 Link Image
Enzyme 6 Chromosome Location 2
Enzyme 6 Locus 22q11.23
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available